data_26557 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Disordered monomeric alpha-synuclein in 20 mM HEPES buffer (pH 7) ; _BMRB_accession_number 26557 _BMRB_flat_file_name bmr26557.str _Entry_type original _Submission_date 2015-04-13 _Accession_date 2015-04-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Wayne . . 2 Insley Thomas . . 3 Tuttle Marcus D. . 4 Zhu Lingyang . . 5 Berthold Deborah A. . 6 Kral Petr . . 7 Rienstra Chad M. . 8 Murphy Catherine J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 113 "13C chemical shifts" 237 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-08-24 original BMRB . stop_ _Original_release_date 2015-04-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Control of protein orientation on gold nanoparticles ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28626495 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Wayne . . 2 Insley Thomas . . 3 Tuttle Marcus D. . 4 Zhu Lingyang . . 5 Berthold Deborah A. . 6 Kral Petr . . 7 Rienstra Chad M. . 8 Murphy Catherine J. . stop_ _Journal_abbreviation 'J Phys Chem C Nanomater Interfaces' _Journal_name_full 'The journal of physical chemistry. C, Nanomaterials and interfaces' _Journal_volume 119 _Journal_issue 36 _Journal_ISSN 1932-7447 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 21035 _Page_last 21043 _Year 2015 _Details . loop_ _Keyword 'alpha synuclein' 'gold nanoparticles' 'protein adsorption' 'surface chemistry' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name alpha-synuclein _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label alpha-synuclein $alpha_synuclein stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_alpha_synuclein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alpha_synuclein _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYV GSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASP 3 3 VAL 4 4 PHE 5 5 MET 6 6 LYS 7 7 GLY 8 8 LEU 9 9 SER 10 10 LYS 11 11 ALA 12 12 LYS 13 13 GLU 14 14 GLY 15 15 VAL 16 16 VAL 17 17 ALA 18 18 ALA 19 19 ALA 20 20 GLU 21 21 LYS 22 22 THR 23 23 LYS 24 24 GLN 25 25 GLY 26 26 VAL 27 27 ALA 28 28 GLU 29 29 ALA 30 30 ALA 31 31 GLY 32 32 LYS 33 33 THR 34 34 LYS 35 35 GLU 36 36 GLY 37 37 VAL 38 38 LEU 39 39 TYR 40 40 VAL 41 41 GLY 42 42 SER 43 43 LYS 44 44 THR 45 45 LYS 46 46 GLU 47 47 GLY 48 48 VAL 49 49 VAL 50 50 HIS 51 51 GLY 52 52 VAL 53 53 ALA 54 54 THR 55 55 VAL 56 56 ALA 57 57 GLU 58 58 LYS 59 59 THR 60 60 LYS 61 61 GLU 62 62 GLN 63 63 VAL 64 64 THR 65 65 ASN 66 66 VAL 67 67 GLY 68 68 GLY 69 69 ALA 70 70 VAL 71 71 VAL 72 72 THR 73 73 GLY 74 74 VAL 75 75 THR 76 76 ALA 77 77 VAL 78 78 ALA 79 79 GLN 80 80 LYS 81 81 THR 82 82 VAL 83 83 GLU 84 84 GLY 85 85 ALA 86 86 GLY 87 87 SER 88 88 ILE 89 89 ALA 90 90 ALA 91 91 ALA 92 92 THR 93 93 GLY 94 94 PHE 95 95 VAL 96 96 LYS 97 97 LYS 98 98 ASP 99 99 GLN 100 100 LEU 101 101 GLY 102 102 LYS 103 103 ASN 104 104 GLU 105 105 GLU 106 106 GLY 107 107 ALA 108 108 PRO 109 109 GLN 110 110 GLU 111 111 GLY 112 112 ILE 113 113 LEU 114 114 GLU 115 115 ASP 116 116 MET 117 117 PRO 118 118 VAL 119 119 ASP 120 120 PRO 121 121 ASP 122 122 ASN 123 123 GLU 124 124 ALA 125 125 TYR 126 126 GLU 127 127 MET 128 128 PRO 129 129 SER 130 130 GLU 131 131 GLU 132 132 GLY 133 133 TYR 134 134 GLN 135 135 ASP 136 136 TYR 137 137 GLU 138 138 PRO 139 139 GLU 140 140 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $alpha_synuclein Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $alpha_synuclein 'recombinant technology' . Escherichia coli . 'pET28-a-synuclein-wild type' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha_synuclein 6.6 mg/mL '[U-100% 13C; U-100% 15N]' HEPES 20 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Agient . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model VNMRS _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-15N_SOFAST_HMQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N SOFAST HMQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D HNCACB' '3D HN(COCA)CB' '2D 1H-15N SOFAST HMQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name alpha-synuclein _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 ASP CA C 54.2 . . 2 2 2 ASP CB C 41.4 . . 3 3 3 VAL H H 8.33 . . 4 3 3 VAL CA C 62.5 . . 5 3 3 VAL CB C 32.6 . . 6 3 3 VAL N N 120.6 . . 7 4 4 PHE H H 8.42 . . 8 4 4 PHE CA C 58.1 . . 9 4 4 PHE CB C 39.2 . . 10 4 4 PHE N N 123.8 . . 11 5 5 MET H H 8.28 . . 12 5 5 MET CA C 55.3 . . 13 5 5 MET CB C 32.6 . . 14 5 5 MET N N 122.7 . . 15 6 6 LYS H H 8.35 . . 16 6 6 LYS CA C 56.8 . . 17 6 6 LYS CB C 32.9 . . 18 6 6 LYS N N 122.9 . . 19 7 7 GLY H H 8.49 . . 20 7 7 GLY CA C 45.2 . . 21 7 7 GLY N N 110.0 . . 22 8 8 LEU H H 8.14 . . 23 8 8 LEU CA C 55.1 . . 24 8 8 LEU CB C 42.4 . . 25 8 8 LEU N N 121.6 . . 26 9 9 SER H H 8.40 . . 27 9 9 SER CA C 58.3 . . 28 9 9 SER CB C 63.7 . . 29 9 9 SER N N 116.9 . . 30 10 10 LYS H H 8.56 . . 31 10 10 LYS CA C 56.2 . . 32 10 10 LYS CB C 32.7 . . 33 10 10 LYS N N 123.6 . . 34 11 11 ALA H H 8.37 . . 35 11 11 ALA CA C 52.6 . . 36 11 11 ALA CB C 19.1 . . 37 11 11 ALA N N 125.5 . . 38 12 12 LYS H H 8.42 . . 39 12 12 LYS CA C 56.8 . . 40 12 12 LYS CB C 32.9 . . 41 12 12 LYS N N 121.1 . . 42 14 14 GLY CA C 45.2 . . 43 15 15 VAL H H 8.04 . . 44 15 15 VAL CA C 62.3 . . 45 15 15 VAL CB C 32.7 . . 46 15 15 VAL N N 120.4 . . 47 16 16 VAL H H 8.39 . . 48 16 16 VAL CA C 62.2 . . 49 16 16 VAL CB C 32.7 . . 50 16 16 VAL N N 125.6 . . 51 18 18 ALA CA C 52.8 . . 52 18 18 ALA CB C 18.9 . . 53 19 19 ALA H H 8.34 . . 54 19 19 ALA CA C 52.8 . . 55 19 19 ALA CB C 19.0 . . 56 19 19 ALA N N 123.2 . . 57 20 20 GLU H H 8.38 . . 58 20 20 GLU CA C 56.8 . . 59 20 20 GLU CB C 30.1 . . 60 20 20 GLU N N 120.2 . . 61 21 21 LYS CA C 56.7 . . 62 21 21 LYS CB C 32.8 . . 63 22 22 THR H H 8.21 . . 64 22 22 THR CA C 62.4 . . 65 22 22 THR CB C 69.7 . . 66 22 22 THR N N 115.6 . . 67 24 24 GLN CA C 56.4 . . 68 24 24 GLN CB C 29.3 . . 69 25 25 GLY H H 8.54 . . 70 25 25 GLY CA C 45.2 . . 71 25 25 GLY N N 110.6 . . 72 26 26 VAL H H 8.08 . . 73 26 26 VAL CA C 62.7 . . 74 26 26 VAL CB C 32.6 . . 75 26 26 VAL N N 120.1 . . 76 27 27 ALA H H 8.48 . . 77 27 27 ALA CA C 52.8 . . 78 27 27 ALA CB C 18.9 . . 79 27 27 ALA N N 127.3 . . 80 28 28 GLU H H 8.47 . . 81 28 28 GLU CA C 56.9 . . 82 28 28 GLU CB C 30.1 . . 83 28 28 GLU N N 120.6 . . 84 29 29 ALA H H 8.35 . . 85 29 29 ALA CA C 52.8 . . 86 29 29 ALA CB C 19.0 . . 87 29 29 ALA N N 124.9 . . 88 30 30 ALA H H 8.29 . . 89 30 30 ALA CA C 52.8 . . 90 30 30 ALA CB C 19.0 . . 91 30 30 ALA N N 123.0 . . 92 31 31 GLY H H 8.36 . . 93 31 31 GLY CA C 45.3 . . 94 31 31 GLY N N 107.8 . . 95 33 33 THR H H 8.30 . . 96 33 33 THR CA C 61.9 . . 97 33 33 THR CB C 69.9 . . 98 33 33 THR N N 115.8 . . 99 34 34 LYS H H 8.52 . . 100 34 34 LYS CA C 53.2 . . 101 34 34 LYS CB C 33.1 . . 102 34 34 LYS N N 124.0 . . 103 36 36 GLY CA C 45.2 . . 104 37 37 VAL H H 7.97 . . 105 37 37 VAL CA C 62.3 . . 106 37 37 VAL CB C 32.8 . . 107 37 37 VAL N N 120.0 . . 108 38 38 LEU H H 8.36 . . 109 38 38 LEU CA C 54.9 . . 110 38 38 LEU CB C 42.4 . . 111 38 38 LEU N N 126.1 . . 112 39 39 TYR H H 8.36 . . 113 39 39 TYR CA C 57.9 . . 114 39 39 TYR CB C 38.8 . . 115 39 39 TYR N N 122.8 . . 116 40 40 VAL H H 8.16 . . 117 40 40 VAL CA C 62.1 . . 118 40 40 VAL CB C 32.8 . . 119 40 40 VAL N N 123.8 . . 120 41 41 GLY H H 8.07 . . 121 41 41 GLY CA C 45.1 . . 122 41 41 GLY N N 112.3 . . 123 42 42 SER H H 8.21 . . 124 42 42 SER CA C 58.3 . . 125 42 42 SER CB C 63.7 . . 126 42 42 SER N N 115.8 . . 127 43 43 LYS H H 8.46 . . 128 43 43 LYS CA C 56.3 . . 129 43 43 LYS CB C 33.0 . . 130 43 43 LYS N N 123.8 . . 131 44 44 THR H H 8.26 . . 132 44 44 THR CA C 61.8 . . 133 44 44 THR CB C 69.8 . . 134 44 44 THR N N 115.8 . . 135 47 47 GLY CA C 45.2 . . 136 48 48 VAL H H 7.98 . . 137 48 48 VAL CA C 62.5 . . 138 48 48 VAL CB C 32.8 . . 139 48 48 VAL N N 120.1 . . 140 49 49 VAL H H 8.38 . . 141 49 49 VAL CA C 62.2 . . 142 49 49 VAL CB C 32.7 . . 143 49 49 VAL N N 125.5 . . 144 50 50 HIS H H 8.63 . . 145 50 50 HIS CA C 56.1 . . 146 50 50 HIS CB C 30.5 . . 147 50 50 HIS N N 124.9 . . 148 51 51 GLY H H 8.50 . . 149 51 51 GLY CA C 45.0 . . 150 51 51 GLY N N 110.7 . . 151 52 52 VAL H H 8.14 . . 152 52 52 VAL CA C 62.0 . . 153 52 52 VAL CB C 32.9 . . 154 52 52 VAL N N 120.5 . . 155 53 53 ALA H H 8.58 . . 156 53 53 ALA CA C 52.4 . . 157 53 53 ALA CB C 19.2 . . 158 53 53 ALA N N 128.5 . . 159 54 54 THR H H 8.32 . . 160 54 54 THR CA C 62.0 . . 161 54 54 THR CB C 69.9 . . 162 54 54 THR N N 115.3 . . 163 55 55 VAL H H 8.34 . . 164 55 55 VAL CA C 62.2 . . 165 55 55 VAL CB C 32.8 . . 166 55 55 VAL N N 123.5 . . 167 56 56 ALA H H 8.52 . . 168 56 56 ALA CA C 52.5 . . 169 56 56 ALA CB C 19.1 . . 170 56 56 ALA N N 128.5 . . 171 57 57 GLU H H 8.45 . . 172 57 57 GLU CA C 56.5 . . 173 57 57 GLU CB C 30.2 . . 174 57 57 GLU N N 121.1 . . 175 58 58 LYS H H 8.52 . . 176 58 58 LYS CA C 56.4 . . 177 58 58 LYS CB C 33.1 . . 178 58 58 LYS N N 123.2 . . 179 59 59 THR H H 8.30 . . 180 59 59 THR CA C 62.1 . . 181 59 59 THR CB C 69.7 . . 182 59 59 THR N N 116.1 . . 183 60 60 LYS H H 8.47 . . 184 60 60 LYS CA C 56.5 . . 185 60 60 LYS CB C 32.9 . . 186 60 60 LYS N N 123.9 . . 187 62 62 GLN CA C 55.6 . . 188 62 62 GLN CB C 29.5 . . 189 63 63 VAL H H 8.37 . . 190 63 63 VAL CA C 62.2 . . 191 63 63 VAL CB C 32.7 . . 192 63 63 VAL N N 122.3 . . 193 64 64 THR H H 8.38 . . 194 64 64 THR CA C 62.1 . . 195 64 64 THR CB C 69.9 . . 196 64 64 THR N N 118.5 . . 197 65 65 ASN H H 8.59 . . 198 65 65 ASN CA C 53.0 . . 199 65 65 ASN CB C 38.8 . . 200 65 65 ASN N N 122.0 . . 201 66 66 VAL H H 8.33 . . 202 66 66 VAL CA C 62.7 . . 203 66 66 VAL CB C 32.4 . . 204 66 66 VAL N N 121.1 . . 205 67 67 GLY H H 8.64 . . 206 67 67 GLY CA C 45.2 . . 207 67 67 GLY N N 112.9 . . 208 68 68 GLY H H 8.29 . . 209 68 68 GLY CA C 44.9 . . 210 68 68 GLY N N 108.9 . . 211 69 69 ALA H H 8.23 . . 212 69 69 ALA CA C 52.2 . . 213 69 69 ALA CB C 19.3 . . 214 69 69 ALA N N 123.8 . . 215 70 70 VAL H H 8.32 . . 216 70 70 VAL CA C 62.3 . . 217 70 70 VAL CB C 32.7 . . 218 70 70 VAL N N 120.9 . . 219 71 71 VAL H H 8.50 . . 220 71 71 VAL CA C 62.1 . . 221 71 71 VAL CB C 32.7 . . 222 71 71 VAL N N 126.0 . . 223 72 72 THR H H 8.40 . . 224 72 72 THR CA C 61.9 . . 225 72 72 THR CB C 69.8 . . 226 72 72 THR N N 119.3 . . 227 73 73 GLY H H 8.51 . . 228 73 73 GLY CA C 45.1 . . 229 73 73 GLY N N 111.5 . . 230 74 74 VAL H H 8.16 . . 231 74 74 VAL CA C 62.3 . . 232 74 74 VAL CB C 32.8 . . 233 74 74 VAL N N 119.9 . . 234 75 75 THR H H 8.39 . . 235 75 75 THR CA C 62.0 . . 236 75 75 THR CB C 69.7 . . 237 75 75 THR N N 119.6 . . 238 76 76 ALA H H 8.47 . . 239 76 76 ALA CA C 52.4 . . 240 76 76 ALA CB C 19.2 . . 241 76 76 ALA N N 127.7 . . 242 77 77 VAL H H 8.25 . . 243 77 77 VAL CA C 62.2 . . 244 77 77 VAL CB C 32.8 . . 245 77 77 VAL N N 120.5 . . 246 78 78 ALA H H 8.51 . . 247 78 78 ALA CA C 52.5 . . 248 78 78 ALA CB C 19.0 . . 249 78 78 ALA N N 128.5 . . 250 79 79 GLN H H 8.49 . . 251 79 79 GLN CA C 55.5 . . 252 79 79 GLN CB C 29.6 . . 253 79 79 GLN N N 120.6 . . 254 80 80 LYS H H 8.53 . . 255 80 80 LYS CA C 56.3 . . 256 80 80 LYS CB C 33.1 . . 257 80 80 LYS N N 123.6 . . 258 81 81 THR H H 8.38 . . 259 81 81 THR CA C 62.1 . . 260 81 81 THR CB C 69.9 . . 261 81 81 THR N N 117.4 . . 262 82 82 VAL H H 8.40 . . 263 82 82 VAL CA C 62.2 . . 264 82 82 VAL CB C 32.8 . . 265 82 82 VAL N N 123.5 . . 266 83 83 GLU H H 8.66 . . 267 83 83 GLU CA C 56.7 . . 268 83 83 GLU CB C 30.2 . . 269 83 83 GLU N N 125.6 . . 270 84 84 GLY H H 8.60 . . 271 84 84 GLY CA C 45.2 . . 272 84 84 GLY N N 110.9 . . 273 85 85 ALA H H 8.33 . . 274 85 85 ALA CA C 52.8 . . 275 85 85 ALA CB C 19.1 . . 276 85 85 ALA N N 124.0 . . 277 86 86 GLY H H 8.57 . . 278 86 86 GLY CA C 45.1 . . 279 86 86 GLY N N 108.3 . . 280 87 87 SER H H 8.33 . . 281 87 87 SER CA C 58.3 . . 282 87 87 SER CB C 63.8 . . 283 87 87 SER N N 115.6 . . 284 88 88 ILE H H 8.27 . . 285 88 88 ILE CA C 53.7 . . 286 88 88 ILE CB C 46.2 . . 287 88 88 ILE N N 123.0 . . 288 89 89 ALA H H 8.44 . . 289 89 89 ALA CA C 52.5 . . 290 89 89 ALA CB C 19.1 . . 291 89 89 ALA N N 128.4 . . 292 90 90 ALA H H 8.31 . . 293 90 90 ALA CA C 52.5 . . 294 90 90 ALA CB C 19.1 . . 295 90 90 ALA N N 123.6 . . 296 91 91 ALA H H 8.38 . . 297 91 91 ALA CA C 52.6 . . 298 91 91 ALA CB C 19.1 . . 299 91 91 ALA N N 123.7 . . 300 92 92 THR H H 8.19 . . 301 92 92 THR CA C 62.0 . . 302 92 92 THR CB C 69.8 . . 303 92 92 THR N N 113.0 . . 304 93 93 GLY H H 8.38 . . 305 93 93 GLY CA C 45.1 . . 306 93 93 GLY N N 110.8 . . 307 94 94 PHE H H 8.16 . . 308 94 94 PHE CA C 57.8 . . 309 94 94 PHE CB C 39.7 . . 310 94 94 PHE N N 120.5 . . 311 95 95 VAL H H 8.13 . . 312 95 95 VAL CA C 62.0 . . 313 95 95 VAL CB C 33.0 . . 314 95 95 VAL N N 124.3 . . 315 96 96 LYS H H 8.48 . . 316 96 96 LYS CA C 56.4 . . 317 96 96 LYS CB C 33.1 . . 318 96 96 LYS N N 126.9 . . 319 97 97 LYS CB C 33.1 . . 320 98 98 ASP H H 8.48 . . 321 98 98 ASP CA C 54.4 . . 322 98 98 ASP CB C 41.0 . . 323 98 98 ASP N N 121.6 . . 324 99 99 GLN H H 8.43 . . 325 99 99 GLN CA C 55.6 . . 326 99 99 GLN CB C 29.4 . . 327 99 99 GLN N N 120.4 . . 328 100 100 LEU H H 8.39 . . 329 100 100 LEU CA C 55.3 . . 330 100 100 LEU CB C 42.1 . . 331 100 100 LEU N N 123.0 . . 332 101 101 GLY H H 8.55 . . 333 101 101 GLY CA C 45.2 . . 334 101 101 GLY N N 110.0 . . 335 102 102 LYS H H 8.28 . . 336 102 102 LYS CA C 56.1 . . 337 102 102 LYS CB C 33.1 . . 338 102 102 LYS N N 120.9 . . 339 103 103 ASN H H 8.70 . . 340 103 103 ASN CA C 53.2 . . 341 103 103 ASN CB C 38.6 . . 342 103 103 ASN N N 120.1 . . 343 104 104 GLU H H 8.55 . . 344 104 104 GLU CA C 56.6 . . 345 104 104 GLU CB C 30.2 . . 346 104 104 GLU N N 121.5 . . 347 106 106 GLY CA C 44.9 . . 348 107 107 ALA H H 8.17 . . 349 107 107 ALA CA C 50.4 . . 350 107 107 ALA CB C 18.1 . . 351 107 107 ALA N N 125.0 . . 352 108 108 PRO CA C 63.0 . . 353 108 108 PRO CB C 32.0 . . 354 109 109 GLN H H 8.67 . . 355 109 109 GLN CA C 55.6 . . 356 109 109 GLN CB C 29.7 . . 357 109 109 GLN N N 121.5 . . 358 110 110 GLU H H 8.61 . . 359 110 110 GLU CA C 56.6 . . 360 110 110 GLU CB C 30.4 . . 361 110 110 GLU N N 122.9 . . 362 111 111 GLY H H 8.56 . . 363 111 111 GLY CA C 45.2 . . 364 111 111 GLY N N 110.4 . . 365 112 112 ILE H H 8.09 . . 366 112 112 ILE CA C 60.8 . . 367 112 112 ILE CB C 38.6 . . 368 112 112 ILE N N 120.3 . . 369 113 113 LEU H H 8.51 . . 370 113 113 LEU CA C 54.9 . . 371 113 113 LEU CB C 42.3 . . 372 113 113 LEU N N 127.5 . . 373 114 114 GLU H H 8.51 . . 374 114 114 GLU CA C 56.3 . . 375 114 114 GLU CB C 30.4 . . 376 114 114 GLU N N 122.5 . . 377 115 115 ASP H H 8.44 . . 378 115 115 ASP CA C 54.2 . . 379 115 115 ASP CB C 41.0 . . 380 115 115 ASP N N 121.7 . . 381 116 116 MET H H 8.37 . . 382 116 116 MET CA C 53.1 . . 383 116 116 MET CB C 32.6 . . 384 116 116 MET N N 122.3 . . 385 117 117 PRO CA C 62.8 . . 386 117 117 PRO CB C 32.1 . . 387 118 118 VAL H H 8.40 . . 388 118 118 VAL CA C 61.8 . . 389 118 118 VAL CB C 33.0 . . 390 118 118 VAL N N 121.2 . . 391 119 119 ASP H H 8.63 . . 392 119 119 ASP CA C 52.1 . . 393 119 119 ASP CB C 40.9 . . 394 119 119 ASP N N 126.5 . . 395 120 120 PRO C C 32.1 . . 396 120 120 PRO CA C 63.3 . . 397 121 121 ASP H H 8.45 . . 398 121 121 ASP CA C 54.4 . . 399 121 121 ASP CB C 40.8 . . 400 121 121 ASP N N 119.6 . . 401 122 122 ASN H H 8.20 . . 402 122 122 ASN CA C 53.4 . . 403 122 122 ASN CB C 39.3 . . 404 122 122 ASN N N 119.3 . . 405 123 123 GLU H H 8.43 . . 406 123 123 GLU CA C 56.7 . . 407 123 123 GLU CB C 30.1 . . 408 123 123 GLU N N 121.3 . . 409 124 124 ALA H H 8.30 . . 410 124 124 ALA CA C 52.2 . . 411 124 124 ALA CB C 19.1 . . 412 124 124 ALA N N 124.8 . . 413 125 125 TYR H H 8.14 . . 414 125 125 TYR CA C 57.6 . . 415 125 125 TYR CB C 39.1 . . 416 125 125 TYR N N 120.3 . . 417 126 126 GLU H H 8.22 . . 418 126 126 GLU CA C 55.5 . . 419 126 126 GLU CB C 30.8 . . 420 126 126 GLU N N 124.2 . . 421 127 127 MET H H 8.52 . . 422 127 127 MET CA C 56.5 . . 423 127 127 MET CB C 32.8 . . 424 127 127 MET N N 124.2 . . 425 128 128 PRO CA C 62.9 . . 426 128 128 PRO CB C 32.2 . . 427 128 128 PRO N N 122.2 . . 428 129 129 SER H H 8.59 . . 429 129 129 SER CA C 58.2 . . 430 129 129 SER CB C 63.8 . . 431 129 129 SER N N 117.0 . . 432 130 130 GLU H H 8.67 . . 433 130 130 GLU CA C 56.3 . . 434 130 130 GLU CB C 30.3 . . 435 130 130 GLU N N 123.4 . . 436 131 131 GLU CA C 56.8 . . 437 131 131 GLU CB C 30.2 . . 438 132 132 GLY H H 8.50 . . 439 132 132 GLY CA C 45.1 . . 440 132 132 GLY N N 110.2 . . 441 134 134 GLN H H 8.28 . . 442 134 134 GLN CA C 55.2 . . 443 134 134 GLN CB C 29.9 . . 444 134 134 GLN N N 123.0 . . 445 135 135 ASP H H 8.31 . . 446 135 135 ASP CA C 54.2 . . 447 135 135 ASP CB C 41.1 . . 448 135 135 ASP N N 122.0 . . 449 136 136 TYR H H 8.14 . . 450 136 136 TYR CA C 57.5 . . 451 136 136 TYR CB C 39.1 . . 452 136 136 TYR N N 120.7 . . 453 137 137 GLU H H 8.35 . . 454 137 137 GLU CA C 53.5 . . 455 137 137 GLU CB C 30.2 . . 456 137 137 GLU N N 125.6 . . 457 139 139 GLU H H 8.60 . . 458 139 139 GLU CA C 56.5 . . 459 139 139 GLU CB C 30.3 . . 460 139 139 GLU N N 121.8 . . 461 140 140 ALA H H 8.10 . . 462 140 140 ALA CA C 20.1 . . 463 140 140 ALA CB C 53.8 . . 464 140 140 ALA N N 131.2 . . stop_ save_